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In humans, tissues within the liver, small intestine, spleen and kidney contain a cytosolic β-glucosidase (CBG) that hydrolyses various β-d-glycosides. This human enzyme shows significant activity towards many xenobiotics commonly found in the human diet including glycosides of phytoestrogens, flavonoids, simple phenolics and cyanogens and ...
Most of the trehalase enzymes isolated from bacteria have as optimum pH of 6.5–7.5. The trehalase enzyme of Mycobacterium smegmatis is a membrane bound protein. Periplasmic trehalase of Escherichia coli K12 is induced by growth at high osmolarity .
α-N-acetylgalactosaminidase (EC 3.2.1.49) is a glycoside hydrolase from bacteria and animals, also known as nagalase. The human gene that codes for this enzyme is NAGA. Mutations in this gene and the deficiency in α-N-acetylgalactosaminidase activity have been identified as the cause of Schindler disease. [1]
Salicin, a glycoside related to aspirin Chemical structure of oleandrin, a cardiac glycoside. In chemistry, a glycoside / ˈ ɡ l aɪ k ə s aɪ d / is a molecule in which a sugar is bound to another functional group via a glycosidic bond. Glycosides play numerous important roles in living organisms. Many plants store chemicals in the form of ...
Human lysosomal α-glucosidase has been studied for the significance of the Asp-518 and other residues in proximity of the enzyme's active site. It was found that substituting Asp-513 with Glu-513 interferes with posttranslational modification and intracellular transport of α-glucosidase's precursor.
This enzyme is a part of a family of enzymes called glycoside hydrolase family 31 (GH31). This is due to the digestive mechanism of the enzyme. GH31 enzymes undergo what is known as the Koshland double displacement mechanism [11] in which a glycosylation and deglycosylation step occurs, resulting in the retention of the overall configuration of the anomeric center.